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Pulse radiolysis study of zinc(II)-insulin

Abstract

Reactions of e/sup -/sub(aq) with zinc(II)-insulin at pH 6.6 and 9.0 yielded relatively low disulphide anion absorptions, suggesting e/sup -/sub(aq) reacts at other sites than S-S. A similar conclusion was reached for the reaction of COsub(./2) where an even lower yield of disulphide anion was found. However, here the disulphide anion yield increased with 'prepulsing'. Simultaneously the rate constant decreased, implying that a more reactive site was 'cleaned up'. While no reaction of Brsub(./2) with insulin was observed, both OH and Clsub(./2) reacted rapidly and predominantly at the tyrosine residues. The second order rate constants, calculated in terms of insulin monomer concentrations, are reported for e/sup -/sub(aq) COsub(./2) and Clsub(./2). The transient spectra qualitatively support evidence regarding the accessibility of S-S bonds and tyrosine residues in the various forms of insulin as predicted from earlier studies.
Authors:
Elliot, A J; Wilkinson, F; Armstrong, D A [1] 
  1. Calgary Univ., Alberta (Canada). Dept. of Chemistry
Publication Date:
Jul 01, 1980
Product Type:
Journal Article
Reference Number:
AIX-11-561959; EDB-81-006783
Resource Relation:
Journal Name: Int. J. Radiat. Biol.; (United Kingdom); Journal Volume: 38:1
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; INSULIN; RADIOLYSIS; CARBON DIOXIDE; HYDRATION; HYDROXYL RADICALS; PULSED IRRADIATION; REACTION KINETICS; SOLVATED ELECTRONS; ZINC COMPOUNDS; CARBON COMPOUNDS; CARBON OXIDES; CHALCOGENIDES; CHEMICAL RADIATION EFFECTS; CHEMICAL REACTIONS; CHEMISTRY; DECOMPOSITION; ELECTRONS; ELEMENTARY PARTICLES; FERMIONS; HORMONES; IRRADIATION; KINETICS; LEPTONS; OXIDES; OXYGEN COMPOUNDS; PEPTIDE HORMONES; RADIATION CHEMISTRY; RADIATION EFFECTS; RADICALS; SOLVATION; 560114* - Radiation Effects on Biochemicals- In Animals- (-1987)
OSTI ID:
6818148
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: IJRBA
Submitting Site:
INIS
Size:
Pages: 1-10
Announcement Date:

Citation Formats

Elliot, A J, Wilkinson, F, and Armstrong, D A. Pulse radiolysis study of zinc(II)-insulin. United Kingdom: N. p., 1980. Web. doi:10.1080/09553008014550901.
Elliot, A J, Wilkinson, F, & Armstrong, D A. Pulse radiolysis study of zinc(II)-insulin. United Kingdom. doi:10.1080/09553008014550901.
Elliot, A J, Wilkinson, F, and Armstrong, D A. 1980. "Pulse radiolysis study of zinc(II)-insulin." United Kingdom. doi:10.1080/09553008014550901. https://www.osti.gov/servlets/purl/10.1080/09553008014550901.
@misc{etde_6818148,
title = {Pulse radiolysis study of zinc(II)-insulin}
author = {Elliot, A J, Wilkinson, F, and Armstrong, D A}
abstractNote = {Reactions of e/sup -/sub(aq) with zinc(II)-insulin at pH 6.6 and 9.0 yielded relatively low disulphide anion absorptions, suggesting e/sup -/sub(aq) reacts at other sites than S-S. A similar conclusion was reached for the reaction of COsub(./2) where an even lower yield of disulphide anion was found. However, here the disulphide anion yield increased with 'prepulsing'. Simultaneously the rate constant decreased, implying that a more reactive site was 'cleaned up'. While no reaction of Brsub(./2) with insulin was observed, both OH and Clsub(./2) reacted rapidly and predominantly at the tyrosine residues. The second order rate constants, calculated in terms of insulin monomer concentrations, are reported for e/sup -/sub(aq) COsub(./2) and Clsub(./2). The transient spectra qualitatively support evidence regarding the accessibility of S-S bonds and tyrosine residues in the various forms of insulin as predicted from earlier studies.}
doi = {10.1080/09553008014550901}
journal = {Int. J. Radiat. Biol.; (United Kingdom)}
volume = {38:1}
journal type = {AC}
place = {United Kingdom}
year = {1980}
month = {Jul}
}